静脉病毒
蛋白质丝
裂谷热
生物
毒力
病毒学
细胞生物学
病毒
生物物理学
遗传学
基因
布尼亚病毒科
作者
M.S. Barski,Benjamin Brennan,Ona K. Miller,Jonathan Potter,Swetha Vijayakrishnan,David Bhella,J.H. Naismith,Richard M. Elliott,Ulrich Schwarz-Linek
出处
期刊:eLife
[eLife Sciences Publications, Ltd.]
日期:2017-09-15
卷期号:6
被引量:17
摘要
Rift Valley fever phlebovirus (RVFV) is a clinically and economically important pathogen increasingly likely to cause widespread epidemics. RVFV virulence depends on the interferon antagonist non-structural protein (NSs), which remains poorly characterized. We identified a stable core domain of RVFV NSs (residues 83–248), and solved its crystal structure, a novel all-helical fold organized into highly ordered fibrils. A hallmark of RVFV pathology is NSs filament formation in infected cell nuclei. Recombinant virus encoding the NSs core domain induced intranuclear filaments, suggesting it contains all essential determinants for nuclear translocation and filament formation. Mutations of key crystal fibril interface residues in viruses encoding full-length NSs completely abrogated intranuclear filament formation in infected cells. We propose the fibrillar arrangement of the NSs core domain in crystals reveals the molecular basis of assembly of this key virulence factor in cell nuclei. Our findings have important implications for fundamental understanding of RVFV virulence.
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